Swiss-Prot entry
ID E75A_DROME STANDARD; PRT; 1237 AA.
AC P17671;
DT 01-AUG-1990 (Rel. 15, Created)
DT 01-AUG-1990 (Rel. 15, Last sequence update)
DT 01-MAY-2005 (Rel. 47, Last annotation update)
DE Ecdysone-induced protein 75B isoform A (E75-A).
GN Name=Eip75B; Synonyms=NR1D3;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha;
OC Ephydroidea; Drosophilidae; Drosophila.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND ALTERNATIVE SPLICING.
RC STRAIN=Canton-S;
RX MEDLINE=90249727; PubMed=2110921 [NCBI, ExPASy, EBI, Israel, Japan];
RA Segraves W.A., Hogness D.S.;
RT "The E75 ecdysone-inducible gene responsible for the 75B early puff in
RT Drosophila encodes two new members of the steroid receptor
RT superfamily.";
RL Genes Dev. 4:204-219(1990).
RN [2]
RP DEVELOPMENTAL STAGE.
RX MEDLINE=94038699; PubMed=8223281 [NCBI, ExPASy, EBI, Israel, Japan];
RA Huet F., Ruiz C., Richards G.;
RT "Puffs and PCR: the in vivo dynamics of early gene expression during
RT ecdysone responses in Drosophila.";
RL Development 118:613-627(1993).
CC -!- FUNCTION: Implicated in the regulation of ecdysone-triggered gene
CC hierarchies. Probably plays a key role in mediating the regulation
CC of the larval molt by 20-OH-ecdysone.
CC -!- SUBCELLULAR LOCATION: Nuclear (Potential).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A; Synonyms=E75A;
CC IsoId=P17671-1; Sequence=Displayed;
CC Name=B; Synonyms=E75B;
CC IsoId=P17672-1; Sequence=External;
CC Name=C; Synonyms=E75C;
CC IsoId=P13055-1; Sequence=External;
CC -!- DEVELOPMENTAL STAGE: In mid instar larvae salivary glands, low
CC basal levels are observed in puff stage 1. Levels increase in late
CC larvae from puff stages 3-10, then decrease abruptly at stage 11.
CC In prepupae, isoform A is the predominant form during the
CC transition between puff stages 18-19. At puff stage 1, expression
CC is also present in the gut. By stage 3 it is present in the wing
CC disks, Malpighian tubules and the fat body. At stage 11,
CC expression is only present in the gut and wing disks.
CC -!- INDUCTION: The expression of this protein is developmentally
CC regulated and is correlated with the 20-OH-ecdysone induced
CC activity of puff 75B.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily.
CC -!- SIMILARITY: Contains 1 nuclear receptor DNA-binding domain.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; X51548; CAA35923.1; -. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A34598; A34598.
DR HSSP; P20393; 1GA5. [HSSP ENTRY / SWISS-3DIMAGE / PDB]
DR SMR; P17671; 240-323.
DR TRANSFAC; T01367; -.
DR FlyBase; FBgn0000568; Eip75B.
DR GO; GO:0004879; F:ligand-dependent nuclear receptor activity; NAS.
DR GO; GO:0018990; P:ecdysis (sensu Insecta); IMP.
DR GO; GO:0035072; P:ecdysone-mediated induction of salivary gla...; NAS.
DR GO; GO:0007553; P:regulation of ecdysteroid metabolism; IMP.
DR InterPro; IPR000536; Hrmon_recept_lig.
DR InterPro; IPR001723; Stdhrmn_receptor.
DR InterPro; IPR008946; Str_ncl_receptor.
DR InterPro; IPR000324; VitD_receptor.
DR InterPro; IPR001628; Znf_C4steroid.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR PRINTS; PR00350; VITAMINDR.
DR ProDom; PD000035; Znf_C4steroid; 1.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain ]
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
DR CMR; P17671.
DR BLOCKS; P17671.
DR ProtoNet; P17671.
DR ProtoMap; P17671.
DR PRESAGE; P17671.
DR DIP; P17671.
DR ModBase; P17671.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Alternative splicing; Developmental protein; DNA-binding;
KW Metal-binding; Nuclear protein; Receptor; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT DNA_BIND 242 318 Nuclear receptor-type.
FT ZN_FING 245 265 C4-type.
FT ZN_FING 282 306 C4-type.
FT DOMAIN 380 590 Ligand-binding (Potential).
FT DOMAIN 721 729 Poly-Gln.
FT DOMAIN 1041 1077 Ser-rich.
SQ SEQUENCE 1237 AA; 133331 MW; BC59260CFC3E4C70 CRC64;
MLMSADSSDS AKTSVICSTV SASMLAPPAP EQPSTTAPPI LGVTGRSHLE NALKLPPNTS
VSAYYQHNSK LGMGQNYNPE FRSLVAPVTD LDTVPPTGVT MASSSNSPNS SVKLPHSGVI
FVSKSSAVST TDGPTAVLQQ QQPQQQMPQH FESLPHHHPQ QEHQPQQQQQ QHHLQHHPHP
HVMYPHGYQQ ANLHHSGGIA VVPADSRPQT PEYIKSYPVM DTTVASSVKG EPELNIEFDG
TTVLCRVCGD KASGFHYGVH SCEGCKGFFR RSIQQKIQYR PCTKNQQCSI LRINRNRCQY
CRLKKCIAVG MSRDAVRFGR VPKREKARIL AAMQQSTQNR GQQRALATEL DDQPRLLAAV
LRAHLETCEF TKEKVSAMRQ RARDCPSYSM PTLLACPLNP APELQSEQEF SQRFAHVIRG
VIDFAGMIPG FQLLTQDDKF TLLKAGLFDA LFVRLICMFD SSINSIICLN GQVMRRDAIQ
NGANARFLVD STFNFAERMN SMNLTDAEIG LFCAIVLITP DRPGLRNLEL IEKMYSRLKG
CLQYIVAQNR PDQPEFLAKL LETMPDLRTL STLHTEKLVV FRTEHKELLR QQMWSMEDGN
NSDGQQNKSP SGSWADAMDV EAAKSPLGSV SSTESADLDY GSPSSSQPQG VSLPSPPQQQ
PSALASSAPL LAATLSGGCP LRNRANSGSS GDSGAAEMDI VGSHAHLTQN GLTITPIVRH
QQQQQQQQQI GILNNAHSRN LNGGHAMCQQ QQQHPQLHHH LTAGAARYRK LDSPTDSGIE
SGNEKNECKA VSSGGSSSCS SPRSSVDDAL DCSDAAANHN QVVQHPQLSV VSVSPVRSPQ
PSTSSHLKRQ IVEDMPVLKR VLQAPPLYDT NSLMDEAYKP HKKFRALRHR EFETAEADAS
SSTSGSNSLS AGSPRQSPVP NSVATPPPSA ASAAAGNPAQ SQLHMHLTRS SPKASMASSH
SVLAKSLMAE PRMTPEQMKR SDIIQNYLKR ENSTAASSTT NGVGNRSPSS SSTPPPSAVQ
NQQRWGSSSV ITTTCQQRQQ SVSPHSNGSS SSSSSSSSSS SSSSSTSSNC SSSSASSCQY
FQSPHSTSNG TSAPASSSSG SNSATPLLEL QVDIADSAQP LNLSKKSPTP PPSKLHALVA
AANAVQRYPT LSADVTVTAS NGGSSVGGGE SGRQQQSAGE CGLPQSGPER RRAQGNAGGV
RAGGGRWFYA EKWERQRLGV AVQRSRKQDH LERRELN
//